CBF12_SCHPO
ID CBF12_SCHPO Reviewed; 963 AA.
AC O74412;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Transcription factor cbf12;
DE AltName: Full=C-promoter element-binding factor-like protein 12;
GN Name=cbf12; ORFNames=SPCC1223.13;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP INDUCTION, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19101542; DOI=10.1016/j.yexcr.2008.12.001;
RA Prevorovsky M., Grousl T., Stanurova J., Rynes J., Nellen W., Puta F.,
RA Folk P.;
RT "Cbf11 and Cbf12, the fission yeast CSL proteins, play opposing roles in
RT cell adhesion and coordination of cell and nuclear division.";
RL Exp. Cell Res. 315:1533-1547(2009).
CC -!- FUNCTION: Transcription factor which function may be to trigger the
CC increase of adhesion at stationary phase, possibly by counteracting or
CC replacing cbf11 at the respective promoters. May also play a cbf11-
CC antagonistic role in the regulation of a number of other important
CC processes such as extracellular material production, colony
CC morphogenesis, ploidy maintenance, or meiosis.
CC {ECO:0000269|PubMed:19101542}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19101542}.
CC -!- INDUCTION: Expression increases as the cells enter the stationary
CC phase, with a statistically significant peak at the late stationary
CC phase. A similar increase in the mRNA levels is found in the
CC sporulating cells. {ECO:0000269|PubMed:19101542}.
CC -!- SIMILARITY: Belongs to the Su(H) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329672; CAA20882.1; -; Genomic_DNA.
DR PIR; T40873; T40873.
DR RefSeq; NP_588358.1; NM_001023349.2.
DR AlphaFoldDB; O74412; -.
DR SMR; O74412; -.
DR BioGRID; 275691; 11.
DR STRING; 4896.SPCC1223.13.1; -.
DR iPTMnet; O74412; -.
DR MaxQB; O74412; -.
DR PaxDb; O74412; -.
DR PRIDE; O74412; -.
DR EnsemblFungi; SPCC1223.13.1; SPCC1223.13.1:pep; SPCC1223.13.
DR GeneID; 2539119; -.
DR KEGG; spo:SPCC1223.13; -.
DR PomBase; SPCC1223.13; cbf12.
DR VEuPathDB; FungiDB:SPCC1223.13; -.
DR eggNOG; KOG3743; Eukaryota.
DR HOGENOM; CLU_307202_0_0_1; -.
DR InParanoid; O74412; -.
DR OMA; WDITIAV; -.
DR PhylomeDB; O74412; -.
DR PRO; PR:O74412; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:PomBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:1900735; P:positive regulation of flocculation; IMP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:PomBase.
DR InterPro; IPR015350; Beta-trefoil_DNA-bd_dom.
DR InterPro; IPR036358; BTD_sf.
DR InterPro; IPR040159; CLS_fam.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR015351; RBP-J/Cbf11/Cbf12_DNA-bd.
DR PANTHER; PTHR10665; PTHR10665; 1.
DR Pfam; PF09270; BTD; 1.
DR Pfam; PF09271; LAG1-DNAbind; 1.
DR SMART; SM01268; BTD; 1.
DR SMART; SM01267; LAG1_DNAbind; 1.
DR SUPFAM; SSF110217; SSF110217; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..963
FT /note="Transcription factor cbf12"
FT /id="PRO_0000363404"
FT REGION 130..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 108335 MW; 582578F90467EC8F CRC64;
MSPNVQKRPS SEDIKTQEFY DSTRNIRRVA TAIGSINANL ESPQLYSLAK STSLQEPVRI
YGDSVSPAIS SSKAHSTSSV SPYYSEKNES QALNADGTAF ANPSFHSFGL PQEDSQDNTQ
TYSTPYTTMN PSNEMHPYPP ATFENNYSVL PDHSSQPNAY SFTGSNILPT QSPSLNQMQD
YQNLQQNGSS NTTIPSFSSQ HDLSQGLTHQ PVPNHDEYAF SYPYELQRKP LIPAHPVPSF
RPTSALKVNM NSNVPSSDSV RNSSPNQYYA STSKQSIPSQ SQNLQPPQKA SVLGTVNNYR
QYQNSFISLN DYQAAQSNIS SPSSRFPTPY SPSVPFGTYQ EKEKSYSQDH AELSYYQQSP
SMMPPYDRSS VYFQQPLSRT DVPNQSFQQY PTTVDGGSMI PNLYPTSAEQ MGLYPQDSQN
KDTYPKSLVN RPSSAVCEPA RNDSIPMMVY SQPVTIEQRI QYVLSNCHCL SAFYLCMPSL
CQKSYGTERR YLCPPIVLYL LGTTWLNNVT DNLKISAQTL EDKDNPKFAK NIFYYNADGA
LISPETDIAK STYQLTNYNE NTNFDSFPVW GNALLKTIYY TGQGKNDGFG RSTFLQLSVQ
SKTKYFKLEN LRLGVISKPS QKRALMKVSD MSIRHGDCVC LFNRYRAQHN NALFLGTSNV
QRAISKVSLN MKYNSNYFPT TDAPNDAENE GAGLAMANNL WEPFYIFSVD ELNKGNNSNP
SDSRSKVLCS NMVIILVSKI TGVQSPPLIL KKHDNWKVSL SSRAPSEAIN CLSKLAFQCH
ETKRFLYIDE KQSSEISFTS GELEYSDPND PTKATHSVLP WSAMWSIIST QSVRTMFYNE
PIHQNAFHVV PSMPFVKFIR LDENSMFHIY GTGFANDVQI WMAYTRCEVK SINAFKPDTT
LPPDIISDSR FSSRVYACTA NLIELICEIP VCMFEPTVEL SPILLFQYET LFHSGYKWPL
ESH
